Characterization of cyclophilin D in freshwater pearl mussel (<em>Hyriopsis schlegelii</em>)

Xiu-Xiu Liu; Cheng-Yuan Wang; Chun Luo; Jun-Qing Sheng; Di Wu; Bei-Juan Hu; Jun-Hua Wang; Yi-Jiang Hong

doi:10.24272/j.issn.2095-8137.2017.018

Volume 38 Issue 2

Mar. 2017

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Article Navigation > Zoological Research > 2017 > 38(2): 103-109

Xiu-Xiu Liu, Cheng-Yuan Wang, Chun Luo, Jun-Qing Sheng, Di Wu, Bei-Juan Hu, Jun-Hua Wang, Yi-Jiang Hong. Characterization of cyclophilin D in freshwater pearl mussel (Hyriopsis schlegelii). Zoological Research, 2017, 38(2): 103-109. doi: 10.24272/j.issn.2095-8137.2017.018

Citation:

Xiu-Xiu Liu, Cheng-Yuan Wang, Chun Luo, Jun-Qing Sheng, Di Wu, Bei-Juan Hu, Jun-Hua Wang, Yi-Jiang Hong. Characterization of cyclophilin D in freshwater pearl mussel (Hyriopsis schlegelii). Zoological Research, 2017, 38(2): 103-109. doi: 10.24272/j.issn.2095-8137.2017.018

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Characterization of cyclophilin D in freshwater pearl mussel (Hyriopsis schlegelii)

doi: 10.24272/j.issn.2095-8137.2017.018

1 School of Life Sciences, Nanchang University, Nanchang Jiangxi 330031, China;
2 Key Laboratory of Aquatic Animals Resources and Utilization of Jiangxi, Nanchang University, Nanchang Jiangxi 330031, China

Funds: This study was supported by the National Natural Science Foundation of China (31660337), Special Aquatic Products Industry Technology System of Jiangxi (JXARS-10), Scientific and Technological Program of Jiangxi Province (KJLD12001, 20152ACF60013 and 150166), and Natural Science Foundation of Jiangxi Province (20122BAB204016)

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Corresponding author: Yi-Jiang Hong
Received Date: 2016-11-07
Rev Recd Date: 2017-03-07
Publish Date: 2017-03-18

Abstract

Abstract

Cyclophilin D (referred to as HsCypD) was obtained from the freshwater pearl mussel (Hyriopsis schlegelii). The full-length cDNA was 2 671 bp, encoding a protein consisting of 367 amino acids. HsCypD was determined to be a hydrophilic intracellular protein with 10 phosphorylation sites and four tetratricopeptide repeat (TPR) domains, but no signal peptide. The core sequence region YKGCIFHRIIKDFMVQGG is highly conserved in vertebrates and invertebrates. Phylogenetic tree analysis indicated that CypD from all species had a common origin, and HsCypD had the closest phylogenetic relationship with CypD from Lottia gigantea. The constitutive mRNA expression levels of HsCypD exhibited tissue-specific patterns, with the highest level detected in the intestines, followed by the gonads, and the lowest expression found in the hemocytes.
- Hyriopsis schlegelii,
- Cyclophilin D,
- Sequence analysis

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References(33)

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